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Database: UniProt
Entry: Q6CAD2
LinkDB: Q6CAD2
Original site: Q6CAD2 
ID   ATM_YARLI               Reviewed;        2282 AA.
AC   Q6CAD2;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   01-OCT-2014, entry version 75.
DE   RecName: Full=Serine/threonine-protein kinase TEL1;
DE            EC=2.7.11.1;
DE   AltName: Full=ATM homolog;
DE   AltName: Full=DNA-damage checkpoint kinase TEL1;
DE   AltName: Full=Telomere length regulation protein 1;
GN   Name=TEL1; OrderedLocusNames=YALI0D03888g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida
OS   lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Serine/threonine protein kinase which activates
CC       checkpoint signaling upon genotoxic stresses such as ionizing
CC       radiation (IR), ultraviolet light (UV), or DNA replication
CC       stalling, thereby acting as a DNA damage sensor. Recognizes the
CC       substrate consensus sequence [ST]-Q. Phosphorylates histone H2A to
CC       form H2AS128ph (gamma-H2A) at sites of DNA damage, involved in the
CC       regulation of DNA damage response mechanism. Required for the
CC       control of telomere length and genome stability (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Associates with DNA double-strand breaks. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere
CC       {ECO:0000250}. Note=Localizes to nuclear DNA repair foci with
CC       other DNA repair proteins in response to DNA double strand breaks.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. ATM subfamily.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 FAT domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00534}.
CC   -!- SIMILARITY: Contains 1 FATC domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00535}.
CC   -!- SIMILARITY: Contains 1 PI3K/PI4K domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00269}.
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DR   EMBL; CR382130; CAG80568.1; -; Genomic_DNA.
DR   RefSeq; XP_502380.1; XM_502380.1.
DR   ProteinModelPortal; Q6CAD2; -.
DR   STRING; 4952.Q6CAD2; -.
DR   EnsemblFungi; CAG80568; CAG80568; YALI0_D03888g.
DR   GeneID; 2910592; -.
DR   KEGG; yli:YALI0D03888g; -.
DR   eggNOG; COG5032; -.
DR   KO; K04728; -.
DR   OrthoDB; EOG7ZWD92; -.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1070.11; -; 2.
DR   InterPro; IPR003152; FATC.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR014009; PIK_FAT.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF56112; SSF56112; 2.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 1.
DR   PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chromatin regulator; Chromosome; Complete proteome;
KW   DNA damage; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW   Serine/threonine-protein kinase; Telomere; Transferase.
FT   CHAIN         1   2282       Serine/threonine-protein kinase TEL1.
FT                                /FTId=PRO_0000227707.
FT   DOMAIN     1325   1844       FAT. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00534}.
FT   DOMAIN     1965   2282       PI3K/PI4K. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00269}.
FT   DOMAIN     2250   2282       FATC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00534, ECO:0000255|PROSITE-
FT                                ProRule:PRU00535}.
SQ   SEQUENCE   2282 AA;  256251 MW;  8BC1704D61DAAC42 CRC64;
     MVIRGVCDSI SRDIASSAVT GKRHTTQMSI FKTIARGHGR FKARSSRQFI VSTVCELLLA
     RHKDRGSQLI VASNLRLVLS HKPHLEHLLW DHYRRSVACL CRELSALCVN SMEESGLEML
     IQELLLCLDL LTKPKYVGMA ELKHDLWNCI DSMLYKYKEV SEMHVLILSI SVSLFQVVFG
     SDYEICHEMV PSIFAIGTKL FTSKSKAVRE ISLRFLLKME IYLASIFGKT CPVPLDQDRL
     NQIEDHMVEL LQVLKNEYNS SSLQDNDVVF EDEIVLVNSK KTMQFLICKL IAMLEYVLSY
     TLTDGNVKQE EDLHGPRKKP RVSISPETPT LNAISAQIQA FQASKPISEV DKPLASLLSS
     ISGSLDKTTR WKFFSAAKLL AQSPPLSPKN AHDVVFLTKW WTEGVAKLRT RSEDSACVLL
     TTILRQHSSA LDPKLVVSLA SNAESKGPLK YSNVSLEFVT CASQFLISHK ACSQSQWSDW
     LFVVLASEQI GATSSKMMLD TAGLLLASVG CLIRMIETPQ NTLETTTSSI MWKTDFKTTS
     STSGDIELTE CMPSITIRDL KSGFQNYLNE LGDWCESASI DVNVVLPSTV FALVVCAVLD
     RQGTPVGLNS RISDFLAVVT KRVEGGSCDS HVFFEAITLI NRLRHYNLLG DSLCILWDSF
     INGIEKLLNV SQVTENEFDP DSPSGKNIMP DLRLSLLLRG PLKSEPFLLA IFPSDIKQYA
     SCDPGKRLPE LFRYVGQTLL SSYLWDCSPL AKQLVVDLLD VYFKSGMTES SDADDLQRWV
     SRDKFLVGPQ LLYGLMQVST PSEYLNLYSS VAICAAERVS SQDSYHCMDA TLTRMSSAKS
     KSRLVVEEMI VALLSVHREC LSLLPVVIER VKTDMLRQKL DTDSESLVRF CKQTGTDSIL
     DKILSVKVGS CVFEEEGHFS TQQLLCSEDS LQWNTQGPPL DILSRTWPDY SPCTLLMLVR
     GLLNLMLKPR VSFEVPLRLV QLKYVLCLFP KRDLCSPDNY VLQQMVSCLI SFLSHSTVGA
     SVRHLLSELF EVIKLPHLEG YIADLGEQSF FGADVSQLLY LLHPSEPHLC KYIEWVNSGF
     SDPEAFLSVF LHTEISDKLK ATLLKSLDFG VTNMTLLGLM DIVCTKETVS FIKRASKLYS
     FDWEESRVLS LLLGRGYLLF GESSNSAPKT NTETSFWNAL TSEFLTLLRG SDFTAKFAVE
     VCLSKIVTKV QVQVPAELQH VFDSGVLEYT HTDEPTTGWV QKTTLELLGL LGGDFELLIP
     LVRTLSSTSP LLPFIFKWTC LEYCRQGEPS YLSQILSQNS SLVVIETFFF VNSFTAHRTL
     NWQPEIVNSA LTLHLYTEAL YFLEADKACW ASQEIQPSYY DIYQNIDDPD LFYGLKFTPC
     LESALKQLNH ENQNLTCFEY ESGLFDWSVE TGGGESKTDI LSHLSTSGMN GLAYTINSDD
     VYRWKLGLLE DPILETGTDD QTVLSQLRSI VVDEKPVLKS TLSDKYLGMQ YLLYQMQLDA
     NSDYLDRIQP PDGVLDILQF CASAWRTIKT ETASYNGILT LSKLGAVSRE LNNAQISKNC
     AVSLQELSRT ASHISGNVCA ISIASCLWSE AAVSRTTPVE MLKRMLGSIN PGQSPVLASQ
     FCQATVLLTD WSSQARMMSP EKIHRLYIAG ASEYMALIPA GNPKTRMFHV FAKFCETQLH
     SQNYDEQIHN AVMDIERLEG ELANLSRISM TREIKHAQRI SRKSLDRAKE SKLNYERLKA
     MFLDSAVQFY LLSCAVRDSE YHEDVTRLIS LWFGNSHVNF VNERMQDYAL IPSFKLAPLI
     NQLSSKLSYE PNNYFQTLLL DLVSATCKAH PFHCLYQISS LMRTDASPQT ERRIQAAVKV
     WNTVKTQEKT ICRAMEIFTD KCVELANAEW PGKGQKASIN QFPNGSWWQN GLRKLNIPPP
     TAQIPLSLDY TDIPSMNKVL AQVIKAGGIS HPKIMDFQLS DGSVSKALLK GGKDDMRQDA
     IMEQVFCRVN QYFLGDPETR KRGLSIRTYN VVPMGPRAGM IEFVANTESL QAALVPLHEK
     DDWDYLTGRT KMSAVAKESN SRRVEVLEEI YTHVTPVMSQ YFFQNFRSSA QAWFKARTNY
     VRSAAASSML GYILGIGDRH CNNIMIDYKT GQLVHIDLGI SFDQGKNLTV PEKVPFRLTR
     DMVDAMGSVG VDGPFRRCCE LSLGLFREQQ DNILSILNVL RYDPLYSWTM SPKKKQTRSS
     SGSDLSDIKL EESNVTADMC LSGVKGKLAV RLSTEAVVRE LIGEAVSVEN LAVIFHGWTP
     FY
//
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